Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5FH91 (SYI_EHRRG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isoleucine--tRNA ligase

EC=6.1.1.5
Alternative name(s):
Isoleucyl-tRNA synthetase
Short name=IleRS
Gene names
Name:ileS
Ordered Locus Names:ERGA_CDS_05000
OrganismEhrlichia ruminantium (strain Gardel) [Complete proteome] [HAMAP]
Taxonomic identifier302409 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia

Protein attributes

Sequence length1118 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) By similarity. HAMAP-Rule MF_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02003.

Domain

IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)) By similarity. HAMAP-Rule MF_02003

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.

Sequence caution

The sequence CAI27952.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processisoleucyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

aminoacyl-tRNA editing activity

Inferred from electronic annotation. Source: InterPro

isoleucine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11181118Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098544

Regions

Motif64 – 7411"HIGH" region HAMAP-Rule MF_02003
Motif647 – 6515"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6501ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5FH91 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: 1DB03A3249BFB06C

FASTA1,118130,722
        10         20         30         40         50         60 
MCIVKTLHLI THVMKEYNSQ FTEGSDFSLI EEQILEFWKE NNIFKKSIEN RDEKRRFVFY 

        70         80         90        100        110        120 
DGPPFANGLP HYGHLLTGFI KDTVARYKTM AGFRVDRRFG WDCHGLPAEM LAEKELGVSG 

       130        140        150        160        170        180 
KLAIEEFGIE KFNNYCRNSV MKFSREWKQY IDRQSRWVDF ENDYKTMNLS FMESIMWSFY 

       190        200        210        220        230        240 
QLWQKGLIYE SIKIVPYSWA CQTPLSNFET RIDNAYRQKT SKTVTLAFEL LDAPKSLIVD 

       250        260        270        280        290        300 
NITAYKILVW TTTPWTLPCN LALAISPNIK YCGAIINKEM YIFSRAYLKN FEDHCKKNNI 

       310        320        330        340        350        360 
EYLIHSDDIC YLSLEYLSYK PVFNYFIDIK NAFKVLVADF VVEDEGTGIV HMAPGFGEDD 

       370        380        390        400        410        420 
FILCKKQGIP DIDDKDTSKL LATICPIDDG GKFTERISDF VNMHVFDTND QIISILKAKN 

       430        440        450        460        470        480 
LCFKTDQYLH NYPHCWRTDT PLIYRAMSSW YVEVTKIKNR MIDLNKDVNW IPSHIRSGQF 

       490        500        510        520        530        540 
GKWLENAKDW AISRNRFWGT PLPVWKSDNP NYPRIDVYGS IKKVFDDIKA LEEDFDIPID 

       550        560        570        580        590        600 
DLHRPYIDNL VRPNPDDPTG KSMMRRVTDV FDCWFESGSM PYAQLHYPFE NKELFENYFP 

       610        620        630        640        650        660 
ADFITEYVAQ TRGWFYTLFV LSTALFDKPP FKNCICHGVV LDTQGQKLSK RLNNYADPME 

       670        680        690        700        710        720 
IFKQYGSDAM RFLMLSHTVS YGGDLLLDKD GVMVRDVIRN VIKPMWNSYN FFTIYADIDK 

       730        740        750        760        770        780 
VSARVISDLD EVDNIMDKYI MCECISTIQS IFNAMEEFDQ SVGNYGYNIK AACNSIVQFF 

       790        800        810        820        830        840 
EVLNNWYIRR CRSRFWSSEI TKDKVNAYNT LYTVMYYMVK VSAPFLPAIT EAIWQKLNFQ 

       850        860        870        880        890        900 
EEESVHLSLL PNIEHITLKD EDQKNIQYMK LIINICGCVL SIRNVRNIRV RQPLNKITIY 

       910        920        930        940        950        960 
SYNNNNDLFN LPVKYQNILL DEINVKSIVF KSNIEDIASF QLKLNFPELG KRIPEKMKNL 

       970        980        990       1000       1010       1020 
ISLLKSNQWK VLENGQLMLG IREGEYYILE DNEYTLNLKV HSEFASTITL GPNLLGVLVL 

      1030       1040       1050       1060       1070       1080 
DNTLTDELIM EGIARDIVRI IQQSRKDNKF NVSDKIDVVI CTQDKMVKNS VQAWYEYIVQ 

      1090       1100       1110 
QTLSLSLVIH ENLDANNVAE YCKTTMKDRN LTLFIKKL 

« Hide

References

[1]"Comparative genomic analysis of three strains of Ehrlichia ruminantium reveals an active process of genome size plasticity."
Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.
J. Bacteriol. 188:2533-2542(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Gardel.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR925677 Genomic DNA. Translation: CAI27952.1. Different initiation.
RefSeqYP_196426.2. NC_006831.1.

3D structure databases

ProteinModelPortalQ5FH91.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING302409.ERGA_CDS_05000.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI27952; CAI27952; ERGA_CDS_05000.
GeneID3268633.
KEGGerg:ERGA_CDS_05000.
PATRIC20578760. VBIEhrRum72196_0535.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMADWNLSRS.
OrthoDBEOG644ZM1.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycERUM302409:GHVW-527-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_EHRRG
AccessionPrimary (citable) accession number: Q5FH91
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries